Effects of aromatic residues at the ends of transmembrane alpha-helices on helix interactions with lipid bilayers


Mall, S., Broadbridge, R., Sharma, R.P., Lee, A.G. and East, J.M. (2000) Effects of aromatic residues at the ends of transmembrane alpha-helices on helix interactions with lipid bilayers. Biochemistry, 39, (8), 2071-2078. (doi:10.1021/bi992205u).

Download

Full text not available from this repository.

Original Publication URL: http://dx.doi.org/10.1021/bi992205u

Description/Abstract

We have studied the effects of aromatic residues at the ends of peptides of the type Ac-KKGLnWLmKKA-amide on their interactions with lipid bilayers as a function of lipid fatty acyl chain length, physical phase, and charge. Peptide Ac-KKGFL6WL8FKKA-amide (F2L14) incorporated into bilayers of phosphatidylcholines containing monounsaturated fatty acyl chains of lengths C14-C24 at a peptide:lipid molar ratio of 1:100 in contrast to Ac-KKGL7WL9KKA-amide (L16) which did not incorporate at all into dierucoylphosphatidylcholine [di(C24:1)PC]; Ac-KKGYL6WL8YKKA-amide (Y2L14) incorporated partly into di(C24:1)PC. Lipid-binding constants relative to that for dioleoylphosphatidylcholine (C18:1)PC were obtained using a fluorescence quenching method. For Y2L14 and F2L14, relative lipid-binding constants increased with increasing fatty acyl chain length from C14 to C24; strongest binding did not occur at the point where the hydrophobic length of the peptide equalled the hydrophobic thickness of the bilayer. For Ac-KKGYL9WL11YKKA-amide (Y2L20), increasing chain length from C18 to C24 had little effect on relative binding constants. Anionic phospholipids bound more strongly than zwitterionic phospholipids to Y2L14 and Y2L20 but effects of charge were relatively small. In two phase (gel and liquid crystalline) mixtures, all the peptides partitioned more strongly into liquid crystalline than gel phase; effects were independent of the structure of the peptide or of the lipid (dipalmitoylphosphatidylcholine or bovine brain sphingomyelin). Addition of cholesterol had little effect on incorporation of the peptides into lipid bilayers. It is concluded that the presence of aromatic residues at the ends of transmembrane -helices effectively buffers them against changes in bilayer thickness caused either by an increase in the chain length of the phospholipid or by the presence of cholesterol.

Item Type: Article
ISSNs: 0006-2960 (print)
Related URLs:
Subjects: R Medicine > RB Pathology
Q Science > QR Microbiology > QR355 Virology
Q Science > QR Microbiology
Divisions: University Structure - Pre August 2011 > School of Biological Sciences
ePrint ID: 56698
Date Deposited: 21 Aug 2008
Last Modified: 27 Mar 2014 18:39
URI: http://eprints.soton.ac.uk/id/eprint/56698

Actions (login required)

View Item View Item